Samples of WT-insulin and Se-insulin[C6UA, C11UA] were prepared under identical conditions.[31 (link)] Proteins were dissolved in 286 μL TDW filtered and pH was corrected to ca. 3.6 using solutions of NaOH 0.1 M and HCl 0.15 M. Acetonitrile-d3 (ACN-d3) was added to get a final ratio 65%:35%, TDW/ACN-d3. The final concentration of the Se-insulin[C6UA, C11 UA] was 0.93 mM and that of the WT-insulin 0.72 mm . NMR experiments were performed with a Bruker AVII 500 MHz spectrometer operating at a proton frequency of 500.13 MHz, using a 5-mm selective probe equipped with a self-shielded xyz-gradient coil at 27.2 °C. The transmitter frequency was set on the water signal and calibrated at 4.811 ppm. Correlation spectroscopy (COSY)[30 ] experiments were acquired using gradients for water saturation under identical conditions. Spectra were processed and analyzed with TopSpin (Bruker Analytische Messtechnik GmbH) and SPARKY3 software (Figure S6 ).[46 ]
Avii 500 mhz spectrometer
Manufactured by Bruker
The AVII 500 MHz spectrometer is a nuclear magnetic resonance (NMR) spectrometer manufactured by Bruker. It operates at a magnetic field strength of 500 MHz, which is commonly used for the analysis of organic and biological molecules. The core function of this instrument is to detect and measure the magnetic properties of atomic nuclei within a sample, providing detailed information about the chemical structure and composition of the analyzed material.
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2 protocols using avii 500 mhz spectrometer
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NMR analysis of Se-insulin and WT-insulin
2
Structural Comparison of Hirudin Variants
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WT-Hir, Hir(C6U/C14U) and Hir(C6U/C16U) samples were all prepared with identical conditions. Proteins were dissolved in 320 µL of 10% D2O in filtered TDW where the pH was adjusted to 4.5 using solutions of 0.5 M NaOH and 0.1 M HCl. The final ionic strength was approximately 7 mM for all samples. The final concentration of WT-Hir was 1.44 mM, Hir(C6U/C14U) was 1.41 mM and Hir(C6U/C16U) was 0.6 mM.
The experiments were performed under identical conditions on a Bruker AVII 500 MHz spectrometer operating at a proton frequency of 500.13 MHz, using a 5-mm selective probe equipped with a self-shielded XYZ-gradient coil at 18.2 °C. Phase sensitive double quantum filtered correlation spectroscopy (DQF-COSY) experiments57 (link) were acquired using gradients for water saturation. Spectra were processed, analyzed and presented with TopSpin (Bruker Analytische Messtechnik GmbH) and NMRFAM SPARKY software58 (link).
The experiments were performed under identical conditions on a Bruker AVII 500 MHz spectrometer operating at a proton frequency of 500.13 MHz, using a 5-mm selective probe equipped with a self-shielded XYZ-gradient coil at 18.2 °C. Phase sensitive double quantum filtered correlation spectroscopy (DQF-COSY) experiments57 (link) were acquired using gradients for water saturation. Spectra were processed, analyzed and presented with TopSpin (Bruker Analytische Messtechnik GmbH) and NMRFAM SPARKY software58 (link).
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